ID D2S6G2_GEOOG Unreviewed; 536 AA.
AC D2S6G2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000256|HAMAP-Rule:MF_01148};
GN Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148};
GN OrderedLocusNames=Gobs_2703 {ECO:0000313|EMBL:ADB75336.1};
OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB75336.1, ECO:0000313|Proteomes:UP000001382};
RN [1] {ECO:0000313|EMBL:ADB75336.1, ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX PubMed=21304698;
RA Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT 20).";
RL Stand. Genomic Sci. 2:158-167(2010).
RN [2] {ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. {ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) +
CC N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein];
CC Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656,
CC ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01148};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01148}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01148}.
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DR EMBL; CP001867; ADB75336.1; -; Genomic_DNA.
DR RefSeq; WP_012948769.1; NC_013757.1.
DR AlphaFoldDB; D2S6G2; -.
DR STRING; 526225.Gobs_2703; -.
DR KEGG; gob:Gobs_2703; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_0_1_11; -.
DR OrthoDB; 9804277at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001382; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07571; ALP_N-acyl_transferase; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR HAMAP; MF_01148; Lnt; 1.
DR InterPro; IPR004563; Apolipo_AcylTrfase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045378; LNT_N.
DR NCBIfam; TIGR00546; lnt; 1.
DR PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01148}; Lipoprotein {ECO:0000313|EMBL:ADB75336.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000001382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01148}.
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 171..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 247..498
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 54888 MW; 9666006EBE2D9322 CRC64;
MPSAIPTGTL ERPARSSAAA PAAGSRWRPG GQAAWRTLLA AVAGVLLLLA FPGSSLPWLA
PLGPAALALA VSGQRARSGA WLGLVCGLAF FVPLLSWSGI FVGALPWLAL AGAQAAYVAL
LGAASAATSR LPLWPLWAAA LWVGQEALRG RFPFGGFPWG RLGLSQTEGP FLAFAAYGGV
PLVGFAVALT GTLLAAAVLR LVRGGRRTAA LAALGAVAVP ALGGLAWLPL PGSSLTAGGP
TRTVAVVQGD VPQPGLEFNE RRRAVLDNHV GQTIGLAEAV AAGEQPQPDL VVWPENSSDI
DPYRNADAAR EISRAADAID APVLVGAVVS GPGEFISNTA IVWAPGTGPG DTYVKRHPVP
FAEYIPFRDF FRLFSDKVDL VRRDFTAGDE VGLLNVGGAR IADVICFEVV YDGLVHDAVS
AGAGMVVVQT NNATFGYSAE SEQQVAAARV RAVEFGRSVA LASTSGISAV IAPDGSLAAA
SGLFESAVFV EEIAQRDSRT LAERLGAGPE WLLSALGAGA LLAVAVPGLR RRGGAG
//
